Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KXK39650.1 | acpP | UZ09_BCD002000800 | UZ09_BCD002000811 | Peptidyl-prolyl isomerase. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.778 |
| KXK39650.1 | nuoD | UZ09_BCD002000800 | UZ09_BCD002001593 | Peptidyl-prolyl isomerase. | NADH dehydrogenase I subunit D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.999 |
| KXK40659.1 | KXK40706.1 | UZ09_BCD002000291 | UZ09_BCD002000194 | Processing peptidase. | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.809 |
| KXK40659.1 | KXK40707.1 | UZ09_BCD002000291 | UZ09_BCD002000195 | Processing peptidase. | Cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.769 |
| KXK40659.1 | KXK40709.1 | UZ09_BCD002000291 | UZ09_BCD002000197 | Processing peptidase. | Cytochrome c oxidase subunit III. | 0.779 |
| KXK40659.1 | KXK40710.1 | UZ09_BCD002000291 | UZ09_BCD002000198 | Processing peptidase. | Cytochrome c oxidase subunit III. | 0.779 |
| KXK40659.1 | KXK41070.1 | UZ09_BCD002000291 | UZ09_BCD002000015 | Processing peptidase. | Semialdehyde dehydrogenase NAD-binding protein. | 0.930 |
| KXK40659.1 | acpP | UZ09_BCD002000291 | UZ09_BCD002000811 | Processing peptidase. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.899 |
| KXK40659.1 | nuoD | UZ09_BCD002000291 | UZ09_BCD002001593 | Processing peptidase. | NADH dehydrogenase I subunit D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.999 |
| KXK40706.1 | KXK40659.1 | UZ09_BCD002000194 | UZ09_BCD002000291 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Processing peptidase. | 0.809 |
| KXK40706.1 | KXK40707.1 | UZ09_BCD002000194 | UZ09_BCD002000195 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
| KXK40706.1 | KXK40709.1 | UZ09_BCD002000194 | UZ09_BCD002000197 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c oxidase subunit III. | 0.997 |
| KXK40706.1 | KXK40710.1 | UZ09_BCD002000194 | UZ09_BCD002000198 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c oxidase subunit III. | 0.998 |
| KXK40706.1 | KXK40816.1 | UZ09_BCD002000194 | UZ09_BCD002000150 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Putative Zn-dependent peptidase. | 0.784 |
| KXK40706.1 | KXK40817.1 | UZ09_BCD002000194 | UZ09_BCD002000151 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Peptidase M16 domain-containing protein; Belongs to the peptidase M16 family. | 0.784 |
| KXK40706.1 | KXK41070.1 | UZ09_BCD002000194 | UZ09_BCD002000015 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Semialdehyde dehydrogenase NAD-binding protein. | 0.898 |
| KXK40706.1 | acpP | UZ09_BCD002000194 | UZ09_BCD002000811 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.826 |
| KXK40706.1 | nuoD | UZ09_BCD002000194 | UZ09_BCD002001593 | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | NADH dehydrogenase I subunit D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.999 |
| KXK40707.1 | KXK40659.1 | UZ09_BCD002000195 | UZ09_BCD002000291 | Cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. | Processing peptidase. | 0.769 |
| KXK40707.1 | KXK40706.1 | UZ09_BCD002000195 | UZ09_BCD002000194 | Cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. | OmpA/MotB domain-containing protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.999 |
page 1 of 5